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P14922

- CYC8_YEAST

UniProt

P14922 - CYC8_YEAST

Protein

General transcriptional corepressor CYC8

Gene

CYC8

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 165 (01 Oct 2014)
      Sequence version 2 (05 Oct 2010)
      Previous versions | rss
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    Functioni

    Acts as component of the CYC8-TUP1 corepressor complex which is involved in the repression of many genes in a wide variety of physiological processes including heme-regulated and catabolite repressed genes. May also be involved in the derepression of at least some target genes. The complex is recruited to target genes by interaction with DNA-bound transcriptional repressors, like MATALPHA2, MIG1, RFX1 and SKO1. The complex recruits histone deacetylases to produce a repressive chromatin structure, interacts with hypoacetylated N-terminal tails of histones H3 and H4 that have been programmed for repression by the action of histone deacetylases and interferes directly with the transcriptional machinery by associating with the RNA polymerase II mediator complex.5 Publications

    GO - Molecular functioni

    1. histone deacetylase binding Source: SGD
    2. protein binding Source: IntAct
    3. RNA polymerase II transcription factor binding transcription factor activity involved in negative regulation of transcription Source: SGD
    4. RNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcription Source: SGD

    GO - Biological processi

    1. chromatin remodeling Source: SGD
    2. negative regulation of dipeptide transport by negative regulation of transcription from RNA polymerase II promoter Source: SGD
    3. negative regulation of transcription from RNA polymerase II promoter during mitosis Source: SGD
    4. nucleosome positioning Source: SGD
    5. positive regulation of transcription from RNA polymerase II promoter Source: GOC
    6. regulation of fatty acid biosynthetic process by regulation of transcription from RNA polymerase II promoter Source: SGD
    7. regulation of response to DNA damage stimulus Source: SGD
    8. regulation of transcription from RNA polymerase II promoter in response to osmotic stress Source: SGD

    Keywords - Molecular functioni

    Prion, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29073-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    General transcriptional corepressor CYC8
    Alternative name(s):
    Glucose repression mediator protein CYC8
    Gene namesi
    Name:CYC8
    Synonyms:CRT8, SSN6
    Ordered Locus Names:YBR112C
    ORF Names:YBR0908
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome II

    Organism-specific databases

    SGDiS000000316. CYC8.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: SGD
    2. transcriptional repressor complex Source: SGD

    Keywords - Cellular componenti

    Amyloid, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 966966General transcriptional corepressor CYC8PRO_0000106327Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei429 – 4291Phosphoserine2 Publications
    Modified residuei475 – 4751Phosphothreonine1 Publication
    Modified residuei710 – 7101Phosphoserine1 Publication
    Modified residuei741 – 7411Phosphoserine1 Publication
    Modified residuei768 – 7681Phosphoserine1 Publication
    Modified residuei815 – 8151Phosphoserine2 Publications
    Modified residuei817 – 8171Phosphoserine2 Publications
    Modified residuei866 – 8661Phosphoserine1 Publication
    Modified residuei943 – 9431Phosphoserine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP14922.
    PaxDbiP14922.
    PeptideAtlasiP14922.

    Expressioni

    Gene expression databases

    GenevestigatoriP14922.

    Interactioni

    Subunit structurei

    Associates with TUP1 to form the CYC8-TUP1 (or TUP1-SSN6) corepressor complex that is composed of 4 copies of TUP1 and one copy of CYC8. Interacts with MATALPHA2, CTI6, MIG1, TUP1, SUT1, RFX1, PGD1, HOS1, HOS2 AND RPD3.10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HOS2P530964EBI-18215,EBI-8475
    PGD1P403563EBI-18215,EBI-13268
    RFX1P487432EBI-18215,EBI-15036
    RPD3P325616EBI-18215,EBI-15864
    TUP1P166495EBI-18215,EBI-19654

    Protein-protein interaction databases

    BioGridi32816. 103 interactions.
    DIPiDIP-696N.
    IntActiP14922. 10 interactions.
    MINTiMINT-579675.
    STRINGi4932.YBR112C.

    Structurei

    3D structure databases

    ProteinModelPortaliP14922.
    SMRiP14922. Positions 45-395.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati46 – 7934TPR 1Add
    BLAST
    Repeati80 – 11334TPR 2Add
    BLAST
    Repeati114 – 14734TPR 3Add
    BLAST
    Repeati150 – 18334TPR 4Add
    BLAST
    Repeati187 – 22034TPR 5Add
    BLAST
    Repeati224 – 25734TPR 6Add
    BLAST
    Repeati262 – 29534TPR 7Add
    BLAST
    Repeati296 – 32934TPR 8Add
    BLAST
    Repeati330 – 36334TPR 9Add
    BLAST
    Repeati364 – 39835TPR 10Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni467 – 682216Prion domain (PrD)Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi15 – 3016Poly-GlnAdd
    BLAST

    Domaini

    The prion domain (PrD) is a Gln/Asn (Q/N)-rich domain, which is unstructured in its native, soluble form, and which forms a parallel in-register beta-sheet in its amyloid form.By similarity

    Sequence similaritiesi

    Belongs to the CYC8/SSN6 family.Curated
    Contains 10 TPR repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, TPR repeat

    Phylogenomic databases

    eggNOGiCOG0457.
    GeneTreeiENSGT00410000025758.
    KOiK06665.
    OrthoDBiEOG7NKKW1.

    Family and domain databases

    Gene3Di1.25.40.10. 2 hits.
    InterProiIPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR019734. TPR_repeat.
    [Graphical view]
    PfamiPF00515. TPR_1. 6 hits.
    [Graphical view]
    SMARTiSM00028. TPR. 10 hits.
    [Graphical view]
    PROSITEiPS50005. TPR. 9 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P14922-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNPGGEQTIM EQPAQQQQQQ QQQQQQQQQQ AAVPQQPLDP LTQSTAETWL    50
    SIASLAETLG DGDRAAMAYD ATLQFNPSSA KALTSLAHLY RSRDMFQRAA 100
    ELYERALLVN PELSDVWATL GHCYLMLDDL QRAYNAYQQA LYHLSNPNVP 150
    KLWHGIGILY DRYGSLDYAE EAFAKVLELD PHFEKANEIY FRLGIIYKHQ 200
    GKWSQALECF RYILPQPPAP LQEWDIWFQL GSVLESMGEW QGAKEAYEHV 250
    LAQNQHHAKV LQQLGCLYGM SNVQFYDPQK ALDYLLKSLE ADPSDATTWY 300
    HLGRVHMIRT DYTAAYDAFQ QAVNRDSRNP IFWCSIGVLY YQISQYRDAL 350
    DAYTRAIRLN PYISEVWYDL GTLYETCNNQ LSDALDAYKQ AARLDVNNVH 400
    IRERLEALTK QLENPGNINK SNGAPTNASP APPPVILQPT LQPNDQGNPL 450
    NTRISAQSAN ATASMVQQQH PAQQTPINSS ATMYSNGASP QLQAQAQAQA 500
    QAQAQAQAQA QAQAQAQAQA QAQAQAQAQA QAQAQAHAQA QAQAQAQAQA 550
    QAQAQAQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQLQP LPRQQLQQKG 600
    VSVQMLNPQQ GQPYITQPTV IQAHQLQPFS TQAMEHPQSS QLPPQQQQLQ 650
    SVQHPQQLQG QPQAQAPQPL IQHNVEQNVL PQKRYMEGAI HTLVDAAVSS 700
    STHTENNTKS PRQPTHAIPT QAPATGITNA EPQVKKQKLN SPNSNINKLV 750
    NTATSIEENA KSEVSNQSPA VVESNTNNTS QEEKPVKANS IPSVIGAQEP 800
    PQEASPAEEA TKAASVSPST KPLNTEPESS SVQPTVSSES STTKANDQST 850
    AETIELSTAT VPAEASPVED EVRQHSKEEN GTTEASAPST EEAEPAASRD 900
    AEKQQDETAA TTITVIKPTL ETMETVKEEA KMREEEQTSQ EKSPQENTLP 950
    RENVVRQVEE DENYDD 966
    Length:966
    Mass (Da):107,202
    Last modified:October 5, 2010 - v2
    Checksum:iFC2D0D0C1B181207
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti547 – 5471Q → K in AAA34545. (PubMed:2854095)Curated
    Sequence conflicti547 – 5471Q → K in AAA35103. (PubMed:3316983)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M23440 Genomic DNA. Translation: AAA34545.1.
    M17826 Genomic DNA. Translation: AAA35103.1.
    X66247 Genomic DNA. Translation: CAA46973.1.
    X78993 Genomic DNA. Translation: CAA55615.1.
    Z35981 Genomic DNA. Translation: CAA85069.1.
    BK006936 Genomic DNA. Translation: DAA07232.1.
    PIRiS25365.
    RefSeqiNP_009670.3. NM_001178460.3.

    Genome annotation databases

    EnsemblFungiiYBR112C; YBR112C; YBR112C.
    GeneIDi852410.
    KEGGisce:YBR112C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M23440 Genomic DNA. Translation: AAA34545.1 .
    M17826 Genomic DNA. Translation: AAA35103.1 .
    X66247 Genomic DNA. Translation: CAA46973.1 .
    X78993 Genomic DNA. Translation: CAA55615.1 .
    Z35981 Genomic DNA. Translation: CAA85069.1 .
    BK006936 Genomic DNA. Translation: DAA07232.1 .
    PIRi S25365.
    RefSeqi NP_009670.3. NM_001178460.3.

    3D structure databases

    ProteinModelPortali P14922.
    SMRi P14922. Positions 45-395.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32816. 103 interactions.
    DIPi DIP-696N.
    IntActi P14922. 10 interactions.
    MINTi MINT-579675.
    STRINGi 4932.YBR112C.

    Proteomic databases

    MaxQBi P14922.
    PaxDbi P14922.
    PeptideAtlasi P14922.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YBR112C ; YBR112C ; YBR112C .
    GeneIDi 852410.
    KEGGi sce:YBR112C.

    Organism-specific databases

    SGDi S000000316. CYC8.

    Phylogenomic databases

    eggNOGi COG0457.
    GeneTreei ENSGT00410000025758.
    KOi K06665.
    OrthoDBi EOG7NKKW1.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29073-MONOMER.

    Miscellaneous databases

    NextBioi 971258.

    Gene expression databases

    Genevestigatori P14922.

    Family and domain databases

    Gene3Di 1.25.40.10. 2 hits.
    InterProi IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR019734. TPR_repeat.
    [Graphical view ]
    Pfami PF00515. TPR_1. 6 hits.
    [Graphical view ]
    SMARTi SM00028. TPR. 10 hits.
    [Graphical view ]
    PROSITEi PS50005. TPR. 9 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of the CYC8 gene mediating glucose repression in yeast."
      Trumbly R.J.
      Gene 73:97-111(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Molecular analysis of SSN6, a gene functionally related to the SNF1 protein kinase of Saccharomyces cerevisiae."
      Schultz J., Carlson M.
      Mol. Cell. Biol. 7:3637-3645(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Molecular analysis of yeast chromosome II between CMD1 and LYS2: the excision repair gene RAD16 located in this region belongs to a novel group of double-finger proteins."
      Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.
      Yeast 8:397-408(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. "Complete DNA sequence of yeast chromosome II."
      Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
      , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
      EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    6. "A repeating amino acid motif in CDC23 defines a family of proteins and a new relationship among genes required for mitosis and RNA synthesis."
      Sikorski R.S., Boguski M.S., Goebl M., Hieter P.A.
      Cell 60:307-317(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAINS TPR REPEATS.
    7. "The tetratricopeptide repeats of Ssn6 interact with the homeo domain of alpha 2."
      Smith R.L., Redd M.J., Johnson A.D.
      Genes Dev. 9:2903-2910(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MATALPHA2.
    8. "Repression by SSN6-TUP1 is directed by MIG1, a repressor/activator protein."
      Treitel M.A., Carlson M.
      Proc. Natl. Acad. Sci. U.S.A. 92:3132-3136(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MIG1.
    9. "The Cyc8 (Ssn6)-Tup1 corepressor complex is composed of one Cyc8 and four Tup1 subunits."
      Varanasi U.S., Klis M., Mikesell P.B., Trumbly R.J.
      Mol. Cell. Biol. 16:6707-6714(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    10. "The DNA replication and damage checkpoint pathways induce transcription by inhibition of the Crt1 repressor."
      Huang M., Zhou Z., Elledge S.J.
      Cell 94:595-605(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RFX1.
    11. "Ssn6-Tup1 interacts with class I histone deacetylases required for repression."
      Watson A.D., Edmondson D.G., Bone J.R., Mukai Y., Yu Y., Du W., Stillman D.J., Roth S.Y.
      Genes Dev. 14:2737-2744(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TUP1; HOS2 AND RPD3, FUNCTION OF THE CYC8-TUP1 COMPLEX.
    12. "Hrs1/Med3 is a Cyc8-Tup1 corepressor target in the RNA polymerase II holoenzyme."
      Papamichos-Chronakis M., Conlan R.S., Gounalaki N., Copf T., Tzamarias D.
      J. Biol. Chem. 275:8397-8403(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PGD1, FUNCTION OF THE CYC8-TUP1 COMPLEX.
    13. "A sequence resembling a peroxisomal targeting sequence directs the interaction between the tetratricopeptide repeats of Ssn6 and the homeodomain of alpha 2."
      Smith R.L., Johnson A.D.
      Proc. Natl. Acad. Sci. U.S.A. 97:3901-3906(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MATALPHA2.
    14. "Regulation of the Sko1 transcriptional repressor by the Hog1 MAP kinase in response to osmotic stress."
      Proft M., Pascual-Ahuir A., de Nadal E., Arino J., Serrano R., Posas F.
      EMBO J. 20:1123-1133(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE CYC8-TUP1 COMPLEX.
    15. "SUT1p interaction with Cyc8p(Ssn6p) relieves hypoxic genes from Cyc8p-Tup1p repression in Saccharomyces cerevisiae."
      Regnacq M., Alimardani P., El Moudni B., Berges T.
      Mol. Microbiol. 40:1085-1096(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SUT1.
    16. "Cti6, a PHD domain protein, bridges the Cyc8-Tup1 corepressor and the SAGA coactivator to overcome repression at GAL1."
      Papamichos-Chronakis M., Petrakis T., Ktistaki E., Topalidou I., Tzamarias D.
      Mol. Cell 9:1297-1305(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CTI6.
    17. "Tup1-Ssn6 interacts with multiple class I histone deacetylases in vivo."
      Davie J.K., Edmondson D.G., Coco C.B., Dent S.Y.
      J. Biol. Chem. 278:50158-50162(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HOS1; HOS2 AND RPD3.
    18. "Histone-dependent association of Tup1-Ssn6 with repressed genes in vivo."
      Davie J.K., Trumbly R.J., Dent S.Y.
      Mol. Cell. Biol. 22:693-703(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE CYC8-TUP1 COREPRESSOR COMPLEX.
    19. "Recruitment of Tup1-Ssn6 by yeast hypoxic genes and chromatin-independent exclusion of TATA binding protein."
      Mennella T.A., Klinkenberg L.G., Zitomer R.S.
      Eukaryot. Cell 2:1288-1303(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE CYC8-TUP1 COMPLEX.
    20. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    21. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-815; SER-817 AND SER-943, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    22. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-710, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429; THR-475; SER-768; SER-866 AND SER-943, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "The yeast global transcriptional co-repressor protein Cyc8 can propagate as a prion."
      Patel B.K., Gavin-Smyth J., Liebman S.W.
      Nat. Cell Biol. 11:344-349(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRION FORMATION.
    25. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429; SER-741; SER-815; SER-817 AND SER-943, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCYC8_YEAST
    AccessioniPrimary (citable) accession number: P14922
    Secondary accession number(s): D6VQB2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 165 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    [OCT+] is the prion form of CYC8. [OCT+] is the result of a conformational change of the cellular CYC8 protein that becomes self-propagating and infectious. [OCT+] aggregates sequester soluble CYC8, resulting in increased levels of iso-2-cytochrome c, defects in sporulation and mating, higher levels of invertase derepression and increased flocculation, reminiscent of a partial loss of function of the CYC8-TUP1 corepressor complex. [OCT+] can be cured by GdnHCl and by inactivation of the molecular chaperone HSP104, which is required for [OCT+] propagation. It is speculated that prion properties of transcription factors may generate an optimized phenotypic heterogeneity that buffers yeast populations against diverse environmental insults (PubMed:19219034).1 Publication
    Present with 3890 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome II
      Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

    External Data

    Dasty 3